CIChang 2013

Meiothermus taiwanensis Protein Structure Revealed – Shedding Light on New Drug Designs

A research team led by Associate Research Fellow Dr. Chung-I Chang and Distinguished Research Fellow Dr. Shih-Hsiung Wu from the Institute of Biological Chemistry, Academia Sinica has resolved the structure of a LonC protease from Meiothermus taiwanensis, a domestic bacterium from hot springs in Wu-rai, Taiwan. The findings, which may shed light on new drugs design, were published in August, 2013 in the journal Acta Crystallographica Section D: Biological Crystallography and was selected as the cover article of the issue.

Lon proteases are found in bacteria to help maintain normal functions under severe environments. Cancer cells and pathogenic bacteria are also found to require Lon proteases to live inside the human body. Therefore, Lon protease has a high potential to be targeted in anti-microbial or anti-cancer therapies.

This study demonstrates that the crystals of the Lon C protease from indigenous Taiwanese thermophilic bacterium are suitable for inhibitor soaking and consequently structure-based drug design. One of the inhibitors, Velcade (bortezomib) with its binding mode determined is already a clinically used anti-cancer drug; the results of this study will thus be valuable for designing more specific drugs with less side effects.

Full articles available at: 1. http://dx.doi.org/10.1107/S0907444913008214
2. http://dx.doi.org/10.1107/S090744491301500X

Authors : J.-H. Liao, K. Ihara, C.-I. Kuo, K.-F. Huang, S. Wakatsuki, S.-H. Wu and C.-I. Chang

Updated : 2013.08.09 (Edited from Academia Sinica press release)

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